David B. Sacks, M.B., Ch.B., F.A.C.P.

 

Place of Birth:       
Cape Town, South Africa

Work Address:    
Brigham and Women's Hospital
Thorn 530
75 Francis Street
Boston, MA 02115
Ph:  617-732-6627
Fax:  617-278-6921
Email: dsacks@rics.bwh.harvard.edu

Education:  
1976  MB ChB, University of Cape Town, South Africa

Selected Bibliography

Original Reports:
 

  • Sacks DB, McDonald JM.  Insulin-stimulated phosphorylation of calmodulin by rat liver insulin receptor preparations.  J Biol Chem 1988; 263:2377-2383.
  • Sacks DB, McDonald JM.  The enigma of insulin resistance and hypertension.  Am J Med 1988; 84:1096-1097.
  • Wong ECC, Sacks DB, Laurino JP, McDonald JM.  Characteristics of calmodulin phosphorylation by the insulin receptor kinase.  Endocrinology 1988; 123:1830-1836.
  • Sacks DB, McDonald JM.  Calmodulin as substrate for insulin receptor kinase:  Phosphorylation by receptors from rat skeletal muscle.  Diabetes 1989; 38:84-90.
  • Sacks DB, Glenn KC, McDonald JM.  The carboxyl terminal segment of the c-Ki-ras 2 gene product mediates insulin-stimulated phosphorylation of calmodulin and stimulates insulin-independent autophosphorylation of the insulin receptor.  Biochem Biophys Res Commun 1989; 161:399-405.
  • Sacks DB, Fujita-Yamaguchi Y, Gale RD, McDonald JM.  Tyrosine-specific phosphoryla-tion of calmodulin by the insulin receptor kinase purified from human placenta.  Biochem J 1989; 263:803-812.
  • Fujita-Yamaguchi Y, Sacks DB, McDonald JM, Sahal D, Kathuria S.  Effect of basic polycations and proteins on purified insulin receptor.  Insulin-independent activation of the insulin receptor tyrosine-specific protein kinase by poly(L-lysine).  Biochem J 1989; 263:813-822.
  • Sacks DB, Porter SE, Ladenson JH, McDonald JM.  Monoclonal antibody to calmodulin:  Development, characterization and comparison with polyclonal anti-calmodulin antibodies.  Anal Biochem 1991; 194:369-377.
  • Sacks DB, Davis HW, Sheehan EL, Williams JP, Garcia JGN, McDonald JM.  Phosphorylation by casein kinase II alters the biological activity of calmodulin.  Biochem J 1992; 283:21-24.
  • Sacks DB, Davis HW, Crimmins DL, McDonald JM.  Insulin-stimulated phosphorylation of calmodulin.  Biochem J 1992; 286:211-216.
  • Sacks DB, McDonald JM.  Effects of cationic polypeptides on the activity and substrate interaction of casein kinase II:  A study with calmodulin.  Arch Biochem Biophys 1992; 299:275-280.
  • Sacks DB, Davis HW, Crimmins DL, Persechini A, McDonald JM.  Casein kinase II-catalysed phosphorylation of calmodulin is altered by amino acid deletions in the central helix of calmodulin.  Biochem Biophys Res Commun 1992; 188:754-759.
  • Reddy GP, Reed WC, Sheehan EL, Sacks DB.  Calmodulin-specific monoclonal antibodies inhibit DNA replication in mammalian cells.  Biochemistry 1992; 31:10426-10430.
  • Tanasijevic MJ, Myers MG Jr, Thoma RS, Crimmins DL, White MF, Sacks DB. Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II.  J Biol Chem 1993; 268:18157-18166.
  • Sugawara A, Yen PM, Apriletti JW, Ribeiro RCJ, Sacks DB, Baxter JD, Chin WW.  Phosphorylation selectively increases triiodothyronine receptor homodimer binding to DNA.  J Biol Chem 1994; 269:433-437.
  • Hardy RW, McDonald JM, Remsen E, d'Avignon A, Sacks DB.  The interaction of calmodulin and polylysine as studied by 1H NMR spectroscopy and sedimentation equilibrium centrifugation.  Biochem Biophys Res Commun 1994; 198:309-317.
  • Sacks DB.  Alteration of calmodulin-protein interactions by a monoclonal antibody to calmodulin.  Biochim Biophys Acta 1994; 1206:120-128.
  • Williams JP, Jo H, Sacks DB, Crimmins DL, Thoma RS, Hunnicutt RE, Radding W, Sharma RK, McDonald JM.  Tyrosine-phosphorylated calmodulin has reduced biological activity.  Arch Biochem Biophys 1994; 315:119-126.
  • Benguria A, Perera OH, Pastor MT, Sacks DB, Villalobo A.  Phosphorylation of calmodulin by the epidermal-grow-th-factor-receptor tyrosine kinase.  Eur J Bio-chem 1994; 224:-909-916.
  • Joyal JL, Sacks DB. Insulin-dependent phosphorylation of calmodulin in rat hepatocytes.  J Biol Chem 1994; 269:30039-30048.
  • Antman EM, Grudzien C, Sacks DB.  Evaluation of a rapid bedside assay for the detection of serum cardiac tro-ponin T. JAMA 1995; 273:-1279-1282.
  • Scott MG, Sacks DB.  Current status of US programs for training clinical laboratory scientists and anticipated impact of hea-lth-care reform. Clin Chem 1995; 41:9-34-941.
  • Hughes-Davies L, Sacks D, Rescigno J, Howard S, Harris J.  Serum cardiac troponin T levels during treatment of early-stage breast cancer. J Clin Oncol 1995; 13:2582-2584.
  • Sacks DB, Mazus B, Joyal JL.  The activity of calmodulin is altered by phosphorylation: modulation of calmodulin function by the site of phosphate incorporation.  Biochem J 1995; 312:197-204.
  • Benguria A, Soriano M, Joyal JL, Sacks DB, Villalobo A.  Phosphorylation of calmodulin by plasma-membrane-associated protein kinase(s).  Eur J Biochem 1995; 234:50-58.
  • Joyal JL, Crimmins DL, Thoma RS, Sacks DB.  Identification of insulin-stimulated phosphorylation sites on calmodulin.  Biochemistry 1996; 35:6-267-6275.
  • Munshi HG, Burks DJ, Joyal JL, White MF, Sacks DB.  Ca2+ regulates calmodulin binding to IQ motifs in IRS-1. Biochemistry 1996; 35:1-5883-1588-9.
  • Sacks DB, Lopez MM, Li Z, Kosk-Kosicka D. Analysis of phosphorylation and mutation of tyrosine residues of calmodulin on its activation of the erythrocyte Ca2+ -transporting ATPase.  Eur J Biochem 1996; 239:98-104.
  • Joyal JL, Annan RA, Ho YD, Huddleston ME, Carr SA, Hart MJ, Sacks DB.  Calmodulin modulates the interaction between IQGAP1 and Cdc42:  Identification of IQGAP1 by nanoelectro-spray tandem mass spectrometry.  J Biol Chem 1997; 272:15419-15425.
  • Michel JB, Feron O, Sacks DB, Michel T.  Reciprocal regulation of endothelial nitric-oxide synthase by Ca 2+-calmodulin and caveolin.  J Biol Chem 1997; 272:15583-15586.
  • Nadeau OW, Sacks DB, Carlson GM. Differential affinity cross-linking of phosphorylase kinase conformers by the geometric isomers of phenylenedimaleimide.   J Biol Chem 1997; 272:26196-26201.
  • Nadeau OW, Sacks DB, Carlson GM.  The structural effects of endogenous and exogenous Ca2+ /calmodulin on phosphorylase kinase.  J Biol Chem 1997; 272:26202-26209.
  • Joyal JL, Burks DJ, Pons S, Matter WF, Vlahos CJ, White MF, Sacks DB.  Calmodulin activates phosphatidylinositol 3-kinase.  J Biol Chem 1997; 272:28183-28186.
  • Ho Y-D, Joyal JL, Li Z, Sacks DB.  IQGAP1 integrates Ca2+/calmodulin and Cdc42 signaling. J Biol Chem 1999; 274:464-470.
  • Taules M, Rodriguez-Vilarrupla A, Rius E, Estanyol JM, Casanovas O, Sacks DB, Perez-Paya E, Bachs O, Agell N. Calmodulin binds to p21Cip1 and is involved in the regulation of its nuclear localization. J Biol Chem  1999; 274:24445-24448.
  • Li Z, Kim SH, Higgins JMG, Brenner MB, Sacks DB.  IQGAP1 and calmodulin modulate E-cadherin function. J Biol Chem 1999; 274:37885-37892.
  • Li Z, Joyal JL, Sacks DB.  Binding of IRS proteins to calmodulin is enhanced in insulin resistance.  Biochemistry 2000; 39:5089-5096.
  • Kim SH, Li Z, Sacks DB. E-cadherin-mediated cell-cell attachment activates Cdc42. J Biol Chem 2000; 275: 36999-37005.
  • Li Z, Joyal JL, Sacks DB.  Calmodulin enhances the stability of the estrogen receptor. J Biol Chem. 2001;276:17354-60.
  • Sokol SY, Li Z, Sacks DB.  The effect of IQGAP1 on Xenopus embryonic ectoderm requires Cdc42.  J Biol Chem. 2001;276:48425-30.
  • Briggs MW, Li Z, Sacks DB.  IQGAP1-mediated stimulation of transcriptional co-activation by beta-catenin is modulated by calmodulin.  J Biol Chem. 2002;277:7453-65.
  • Swart-Mataraza JM, Li Z, Sacks DB. IQGAP1 is a component of Cdc42 signaling to the cytoskeleton. J Biol Chem 2002; 277:24753-24763.
  • Li L, Li Z, Sacks DB. Calmodulin regulates the transcriptional activity of estrogen receptors: selective inhibition of calmodulin function in subcellular compartments. J Biol Chem 2003; 278:1195-1200.
  • Li Z, Sacks DB. Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1. J Biol Chem 2003; 278:4347-4352.
  • Soncin F, Zhang X, Chu B, Wang X, Asea A, Stevenson MA, Sacks DB, Calderwood SK. Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. Biochem Biophys Res Commun 2003; 303:700-706.
  • Mataraza JM, Briggs MW, Li Z, Frank R, Sacks DB. Identification and characterization of the Cdc42-binding site of IQGAP1. Biochem Biophys Res Commun 2003; 305:315-321.


Book Chapters/Reviews:
 

  •  Sacks DB, Valdes R Jr.  Gestational diabetes:  Implications for the laboratory.  American Association of Clinical Chemistry.  Washington DC.  Endocrinology and Metabolism, October 1986; 5:5-7, Special feature.
  • Sacks DB, McDonald JM.  The role of calcium and calmodulin in the mechanism of insulin action.  In:  Heilmann C (ed).  Calcium-Dependent Processes in the Liver.  MTP Press, Lancaster, 1988: 31-48.
  • Sacks DB, McDonald JM.  Calcium and insulin action.  In:  Draznin B, Melmed S, LeRoith D (eds).  Molecular and Cellular Biology of Diabetes Mellitus.  Vol. 2. Liss Publishers, New York, 1989: 193-202.
  • Sacks DB.  The mechanism of insulin action.  Clin Biochem 1993; 26:308-311.
  • Sacks DB.  Carbohydrates.  In:  Burtis C, Ashwood E (eds).  Tietz Textbook of Clinical Chemistry. 2nd ed. Saunders, Philadelphia, 1994: 928-1001.
  • Benjamin RJ, Sacks DB.  Glycated protein update:  Implications of recent studies, including the Diabetes Control and Complications Trial.  Clin Chem 1994; 40:683-687.
  • Sacks DB.  Does phosphorylation regulate calmodulin function? Bio-Regulations, 1995; 4:96-102.
  • Sacks DB. Carbohydrates.  In: Burtis C, Ashwood E (eds).  Tietz Fundamentals of Clinical Chemistry. 4th ed. Saunders, Philadelphia, 1996; 351-374.
  • Sacks DB, McDonald JM.  The pathogenesis of type II diabetes mellitus: a polygenic disease. Am J Clin Pathol 1996; 105:-149-156.
  • Sacks DB. Amylin - a glucoregulatory hormone involved in the pathogenesis of diabetes mellitus? [Editorial]. Clin Chem 1996; 42:494-495.
  • Sacks DB. Implications of the revised criteria for the diagnosis and classification of diabetes mellitus [Editorial]. Clin Chem 1997; 43:2230-2232.
  • Sacks DB. Carbohydrates. In: Burtis C, Ashwood E (eds). Tietz Textbook of Clinical Chemistry. 3rd ed. Philadelphia:  WB Saunders, 1999. p.750-808.
  • Chun KC, Sacks DB.  The interaction of calmodulin with novel target proteins.  In:  Pochet R, (ed).  Calcium:  The molecular basis of calcium action in biology and medicine.  Dordrecht:  Kluwer, 2000; p.541-563.
  • Bry L, Chen PC, Sacks DB. Effects of hemoglobin variants and chemically modified derivatives on assays for glycohemoglobin [Review]. Clin Chem 2001; 47:153-163.
  • Sacks DB, Lernmark A. Molecular manipulation of autoantibody testing in type 1 diabetes: two for one [Editorial]. Clin Chem 2001; 47:803-804.
  • Sacks DB, Bruns DE, Goldstein DE, Maclaren NK, McDonald JM, Parrott M. Guidelines and recommendations for laboratory analysis in the diagnosis and management of diabetes mellitus. Clin Chem 2002; 48:436-472. [Published concurrently as Diabetes Care 2002; 25:750-786.]
  • Briggs MW, Sacks DB. IQGAP1 as signal integrator: Ca2+, calmodulin, Cdc42 and the cytoskeleton [Review]. FEBS Lett 2003; 542:7-11.
  • Briggs MW, Sacks DB. IQGAP proteins are integral components of cytoskeletal regulation [Review]. EMBO reports 2003; in the press.